GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters.

TitleGLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters.
Publication TypeJournal Article
Year of Publication2016
AuthorsDeng, D, Yan, N
JournalProtein Sci
Volume25
Issue3
Pagination546-58
Date Published2016 Mar
ISSN1469-896X
KeywordsAnimals, Glucose, Glucose Transport Proteins, Facilitative, Humans, Models, Molecular, Monosaccharide Transport Proteins, Protein Conformation, Sodium-Glucose Transport Proteins, Substrate Specificity
Abstract

Glucose is the primary fuel to life on earth. Cellular uptake of glucose is a fundamental process for metabolism, growth, and homeostasis. Three families of secondary glucose transporters have been identified in human, including the major facilitator superfamily glucose facilitators GLUTs, the sodium-driven glucose symporters SGLTs, and the recently identified SWEETs. Structures of representative members or their prokaryotic homologs of all three families were obtained. This review focuses on the recent advances in the structural elucidation of the glucose transporters and the mechanistic insights derived from these structures, including the molecular basis for substrate recognition, alternating access, and stoichiometric coupling of co-transport.

DOI10.1002/pro.2858
Alternate JournalProtein Sci.
PubMed ID26650681
PubMed Central IDPMC4815417